The association of rhodamine - labelled alpha-actinin with actin bundles in demembranated cells.
Rhodamine-labelled alpha-actinin was specifically bound to actin containing filament bundles of demembranated fibroblasts, and was particularly associated with their termini. Optimal binding of rhodamine-alpha-actinin occurred at pH 6.0 - 6.2 and could be abolished by the addition of unlabeled alpha-actinin or myosin subfragment 1. The spatial relationships between the decorating alpha-actinin and several actin associated proteins was determined by double fluorescence microscopy.
D000185:Actinin / Q000378:metabolism*; D000199:Actins / Q000032:analysis; D000818:Animals; D002460:Cell Line; D002478:Cells, Cultured; D002642:Chick Embryo; D003285:Contractile Proteins / Q000032:analysis; D003599:Cytoskeleton / Q000378:metabolism*; D004285:Dogs; D005347:Fibroblasts; D064448:Filamins; D006863:Hydrogen-Ion Concentration; D008840:Microfilament Proteins; D009124:Muscle Proteins / Q000032:analysis / Q000378:metabolism*; D012235:Rhodamines; D014335:Tropomyosin / Q000032:analysis; D016596:Vinculin
D000199:Actins; D003285:Contractile Proteins; D064448:Filamins; D008840:Microfilament Proteins; D009124:Muscle Proteins; D012235:Rhodamines; D014335:Tropomyosin; D000185:Actinin; D016596:Vinculin